Maturation Kinetics of a Multiprotein Complex Revealed by Metabolic Labeling
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Date
2020-12-23Type
- Journal Article
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Cited 13 times in
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Cited 15 times in
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Abstract
All proteins interact with other cellular components to fulfill their function. While tremendous progress has been made in the identification of protein complexes, their assembly and dynamics remain difficult to characterize. Here, we present a high-throughput strategy to analyze the native assembly kinetics of protein complexes. We apply our approach to characterize the co-assembly for 320 pairs of nucleoporins (NUPs) constituting the ≈50 MDa nuclear pore complex (NPC) in yeast. Some NUPs co-assemble fast via rapid exchange whereas others require lengthy maturation steps. This reveals a hierarchical principle of NPC biogenesis where individual subcomplexes form on a minute timescale and then co-assemble from center to periphery in a ∼1 h-long maturation process. Intriguingly, the NUP Mlp1 stands out as joining very late and associating preferentially with aged NPCs. Our approach is readily applicable beyond the NPC, making it possible to analyze the intracellular dynamics of a variety of multiprotein assemblies. © 2020 Elsevier Inc.
A general approach to determining assembly kinetics for large protein architectures reveals the time scale and assembly sequence for the nuclear pore complex. © 2020 Elsevier Inc. Show more
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publishedExternal links
Journal / series
CellVolume
Pages / Article No.
Publisher
Massachusetts Institute of TechnologyOrganisational unit
09464 - Weis, Karsten / Weis, Karsten
Funding
179275 - Structure and Function of the Nuclear Pore Complex (SNF)
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Show all metadata
Citations
Cited 13 times in
Web of Science
Cited 15 times in
Scopus
ETH Bibliography
yes
Altmetrics